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Protein

Guanylate kinase

Gene

Guk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for recycling GMP and indirectly, cGMP.

Catalytic activityi

ATP + GMP = ADP + GDP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 4411 Publication
Active sitei137 – 13711 Publication
Active sitei148 – 14811 Publication
Binding sitei171 – 1711ATP
Binding sitei172 – 1721ATP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. guanylate kinase activity Source: UniProtKB

GO - Biological processi

  1. ATP metabolic process Source: Ensembl
  2. dATP metabolic process Source: Ensembl
  3. dGDP biosynthetic process Source: Ensembl
  4. dGMP metabolic process Source: Ensembl
  5. GDP biosynthetic process Source: Ensembl
  6. GDP-mannose metabolic process Source: Ensembl
  7. glycoprotein transport Source: Ensembl
  8. GMP metabolic process Source: Ensembl
  9. purine nucleotide metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.4.8. 3474.
ReactomeiREACT_274011. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_329645. Abacavir metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate kinase (EC:2.7.4.8)
Alternative name(s):
GMP kinase
Gene namesi
Name:Guk1
Synonyms:Gmk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95871. Guk1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 198197Guanylate kinasePRO_0000170652Add
BLAST

Proteomic databases

MaxQBiQ64520.
PaxDbiQ64520.
PRIDEiQ64520.

PTM databases

PhosphoSiteiQ64520.

Expressioni

Gene expression databases

BgeeiQ64520.
CleanExiMM_GUK1.
ExpressionAtlasiQ64520. baseline and differential.
GenevestigatoriQ64520.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ64520. 2 interactions.
MINTiMINT-4099756.

Structurei

Secondary structure

1
198
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Helixi17 – 2812Combined sources
Turni29 – 313Combined sources
Beta strandi32 – 343Combined sources
Turni49 – 513Combined sources
Helixi58 – 6710Combined sources
Beta strandi70 – 767Combined sources
Beta strandi79 – 846Combined sources
Helixi85 – 939Combined sources
Beta strandi97 – 1015Combined sources
Helixi104 – 1107Combined sources
Beta strandi118 – 1236Combined sources
Helixi127 – 13711Combined sources
Helixi142 – 15514Combined sources
Helixi156 – 1605Combined sources
Turni162 – 1643Combined sources
Beta strandi166 – 1705Combined sources
Helixi174 – 18411Combined sources
Helixi186 – 1916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LVGX-ray2.10A1-198[»]
ProteinModelPortaliQ64520.
SMRiQ64520. Positions 5-194.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64520.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 186183Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the guanylate kinase family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0194.
HOVERGENiHBG003344.
InParanoidiQ64520.
KOiK00942.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64520-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGPRPVVLS GPSGAGKSTL LKKLFQEHSS IFGFSVSHTT RNPRPGEEDG
60 70 80 90 100
KDYYFVTREM MQRDIAAGDF IEHAEFSGNL YGTSKEAVRA VQAMNRICVL
110 120 130 140 150
DVDLQGVRSI KKTDLCPIYI FVQPPSLDVL EQRLRLRNTE TEESLAKRLA
160 170 180 190
AARTDMESSK EPGLFDLVII NDDLDKAYAT LKQALSEEIK KAQGTGHA
Length:198
Mass (Da):21,918
Last modified:January 22, 2007 - v2
Checksum:iF584E4B6521C607B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53514 mRNA. Translation: AAC52652.1.
BC024625 mRNA. Translation: AAH24625.1.
RefSeqiXP_006532308.1. XM_006532245.2.
XP_006532309.1. XM_006532246.2.
UniGeneiMm.3624.

Genome annotation databases

GeneIDi14923.
KEGGimmu:14923.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53514 mRNA. Translation: AAC52652.1.
BC024625 mRNA. Translation: AAH24625.1.
RefSeqiXP_006532308.1. XM_006532245.2.
XP_006532309.1. XM_006532246.2.
UniGeneiMm.3624.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LVGX-ray2.10A1-198[»]
ProteinModelPortaliQ64520.
SMRiQ64520. Positions 5-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ64520. 2 interactions.
MINTiMINT-4099756.

PTM databases

PhosphoSiteiQ64520.

Proteomic databases

MaxQBiQ64520.
PaxDbiQ64520.
PRIDEiQ64520.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14923.
KEGGimmu:14923.

Organism-specific databases

CTDi2987.
MGIiMGI:95871. Guk1.

Phylogenomic databases

eggNOGiCOG0194.
HOVERGENiHBG003344.
InParanoidiQ64520.
KOiK00942.

Enzyme and pathway databases

BRENDAi2.7.4.8. 3474.
ReactomeiREACT_274011. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_329645. Abacavir metabolism.

Miscellaneous databases

ChiTaRSiGuk1. mouse.
EvolutionaryTraceiQ64520.
PROiQ64520.
SOURCEiSearch...

Gene expression databases

BgeeiQ64520.
CleanExiMM_GUK1.
ExpressionAtlasiQ64520. baseline and differential.
GenevestigatoriQ64520.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, characterization, and modeling of mouse and human guanylate kinases."
    Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.
    J. Biol. Chem. 271:16734-16740(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. "Structural characterization of the closed conformation of mouse guanylate kinase."
    Sekulic N., Shuvalova L., Spangenberg O., Konrad M., Lavie A.
    J. Biol. Chem. 277:30236-30243(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), ATP-BINDING SITES, ACTIVE SITE.

Entry informationi

Entry nameiKGUA_MOUSE
AccessioniPrimary (citable) accession number: Q64520
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.